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Preferential Radioassay of Influenza-Specific 7S (IgG) Over 19S (IgM) Class of Antibodies

From the Center for Disease Control, Health Services and Mental Health Administration, Public Health Service, United States Department of Health, Education, and Welfare, Atlanta, Georgia 30333

Abstract

Binding affinities of immunoglobulins for A2 Hong Kong influenza viral antigen have been studied as another aspect of antibody heterogeneity. Immunoglobulin G (IgG) binding exceeds immunoglobulin M (IgM) binding in antigen-antibody reactions of precipitation, dissociation, and absorption. Evidence now indicates that IgG is more active than IgM in solid phase radioimmunoassay (RIA) inhibition as well. The preferential binding capacity of either 7S (IgG) or 19S (IgM) radioiodine-labeled globulin was quantitated with the other globulin serving as inhibitor. The range of ratios of concentrations of 7S and 19S globulins indicated that at a 7S/19S weight ratio of approximately five, the inhibition of 19S by 7S globulins appeared to be almost complete. Serologically negative 7S globulins had no such effect upon binding of 19S globulins. Conversely, the effect of serologically positive 19S globulins upon binding of 7S globulins was not apparent even at a 5-fold ratio of 19S globulin concentration. Alternatively, binding of the 7S globulins could be completely inhibited by preincubating the 7S globulins with anti-IgG before solid-phase RIA.